Reviewed, UniProtKB/Swiss-Prot Q0VQ06 (SYS_ALCBS)

Names and origin

Protein names

Recommended name:
    Seryl-tRNA synthetase
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
      Short name=SerRS

Gene names

Name:	serS
Ordered Locus Names:	ABO_1294

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) By similarity.
Catalytic activity	ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_00176 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_00176
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_00176
Subunit structure	Homodimer. The tRNA molecule binds across the dimer By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP seryl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP serine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 429	429	Seryl-tRNA synthetase HAMAP MF_00176		PRO_1000019606
Regions
	Nucleotide binding	267 – 269	3	ATP By similarity
	Nucleotide binding	354 – 357	4	ATP By similarity
	Region	236 – 238	3	Serine binding By similarity
Sites
	Binding site	290	1	Serine By similarity
	Binding site	390	1	Serine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VQ06-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 2EC992A74F72D5BB	FASTA	429	47,944
	10 20 30 40 50 60 MLDIRALRQD GEAIKAALSK RGYTLDLEEF AALDAKRKQA DMRSQELQAD RKKASKQVGE 70 80 90 100 110 120 LIKSGMAVDE AKAQVADALQ TIDTELDKEV ASAKAIQDEI REYLMGIPNV PQEAVPAGND 130 140 150 160 170 180 EDDNVEVRRW GTPKTLPFEP KDHVDIGEAL EGGLDFERAA KLSGARFAVM SGGLARMHRA 190 200 210 220 230 240 LIDFMLDIHS DEHGYQEVYV PFLVGPEALR GTGQLPKFAE DLFKIEGERE LYLIPTAEVP 250 260 270 280 290 300 VTNLAADEIL EANTMPRRYT CHTPCFRSEA GSHGRDTRGM IRQHQFEKVE LVQMVRPEES 310 320 330 340 350 360 DAALEALTGH AEAILQKLDL PYRVVILCGG DLGFSSSKTY DIEVWLPSQQ CYREISSCSN 370 380 390 400 410 420 FRDYQSRRMQ ARWRNPETGK PELVHTLNGS ALAVGRTLVA ILENYQNDDG SVTVPEALRP YMRGLERLK

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL16742.1.
RefSeq	YP_693014.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4213632.
GenomeReviews	Gene locus ABO_1294 in contig AM286690_GR.
KEGG	abo:ABO_1294.
NMPDR	fig|393595.12.peg.1306.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VQ06.
OMA	Q0VQ06. LKPYMGG.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_1294-MON.
Family and domain databases
HAMAP	MF_00176. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. IPR015866. Ser-tRNA-synth_IIa_N. [Graphical view]
Gene3D	G3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
PANTHER	PTHR11778. tRNA-synt_ser. 1 hit.
Pfam	PF02403. Seryl_tRNA_N. 1 hit. PF00587. tRNA-synt_2b. 1 hit. [Graphical view]
PIRSF	PIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTS	PR00981. TRNASYNTHSER.
TIGRFAMs	TIGR00414. serS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYS_ALCBS

Accession

Primary (citable) accession number: Q0VQ06

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)